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Article

Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds.

Biochemistry - 8 May 1990

Hurle M R, Marks C B, Kosen P A, Anderson S, Kuntz I D

Abstract excerpt

The equilibrium and kinetic behavior of the guanidine hydrochloride (Gdn-HCl) induced unfolding/refolding of four bovine pancreatic trypsin inhibitor (BPTI) mutants was examined by using ultraviolet difference spectroscopy. In three of the mutants, we replaced the buried 30-51 disulfide bond with alanine at position 51 and valine (Val30/Ala51), alanine (Ala30/Ala51), or threonine (Thr30/Ala51) at position 30. For...

Topics

Amino Acid Sequence
Animals
Aprotinin
Cattle
Disulfides
Escherichia coli
Genes
Guanidine
Guanidines
Kinetics
Mutation
Plasmids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Protein Denaturation

Source

Identifiers

PMID: 1693524
DOI: 10.1021/bi00470a021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1693524-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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